Supplementary Materials

Supplementary Material for:

The proinflammatory role of HECTD2 in innate immunity and experimental lung injury

Tiffany A. Coon, Alison C. McKelvey, Travis Lear, Shristi Rajbhandari, Sarah R. Dunn, William Connelly, Joe Y. Zhao, SeungHye Han, Yuan Liu, Nathaniel M. Weathington, Bryan J. McVerry, Yingze Zhang, Bill B. Chen*

*Corresponding author. E-mail: chenb{at}upmc.edu

Published 8 July 2015, Sci. Transl. Med. 7, 295ra109 (2015)
DOI: 10.1126/scitranslmed.aab3881

This PDF file includes:

  • Fig. S1. PIAS1 degradation occurs in a ubiquitin-dependent manner and through the proteasome.
  • Fig. S2. K30 is the ubiquitin acceptor site within PIAS1.
  • Fig. S3. Deletional mapping study identifying PIAS1 binding site within HECTD2.
  • Fig. S4. R397 is the preferred binding site for PIAS1.
  • Fig. S5. HECTD2 interacts with the first 20 amino acids of PIAS1.
  • Fig. S6. HECTD2A19P and deletional mutant localization study.
  • Fig. S7. FRET study of HECTD2 chimera proteins with PIAS1.
  • Fig. S8. BC1382 exhibits anti-inflammatory activity through preservation of PIAS1.
  • Fig. S9. BC1382 ameliorates LPS-induced lung injury.
  • Fig. S10. Source data for Fig. 1 (A to D and H).
  • Fig. S11. Source data for Fig. 2 (A to K).
  • Fig. S12. Source data for Fig. 3 (A to F).
  • Fig. S13. Source data for Figs. 4H, 5C, 6I, and 7 (C and I).
  • Table S1. Source sequencing data for Table 3.
  • Table S2. Source data for Fig. 1 (E to G).
  • Table S3. Source data for Fig. 3G.
  • Table S4. Source data for Fig. 4 (A to F).
  • Table S5. Source data for Fig. 5 (A, B, and D to F).
  • Table S6. Source data for Fig. 6 (A to G).
  • Table S7. Source data for Fig. 7 (C to G).

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